[1]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Kidney; PubMed=1313579 [NCBI, ExPASy, EBI, Israel, Japan] Williams M.K., Kantrowitz E.R.; "Isolation and sequence analysis of the cDNA for pig kidney fructose 1,6-bisphosphatase."; Proc. Natl. Acad. Sci. U.S.A. 89:3080-3082(1992).
[2]	PROTEIN SEQUENCE OF 2-336. TISSUE=Kidney cortex; PubMed=6296821 [NCBI, ExPASy, EBI, Israel, Japan] Marcus F., Edelstein I., Reardon I., Heinrikson R.L.; "Complete amino acid sequence of pig kidney fructose-1,6-bisphosphatase."; Proc. Natl. Acad. Sci. U.S.A. 79:7161-7165(1982).
[3]	PROTEIN SEQUENCE OF 2-24 AND 44-61. TISSUE=Kidney; DOI=10.1016/0003-9861(82)90547-1; PubMed=6291465 [NCBI, ExPASy, EBI, Israel, Japan] McGregor J.S., Hannappel E., Xu G.-J., Pontremoli S., Horecker B.L.; "Conservation of primary structure at the proteinase-sensitive site of fructose 1,6-bisphosphatases."; Arch. Biochem. Biophys. 217:652-664(1982).
[4]	SUBSTRATE-BINDING SITE, LIGANDS, AND REVIEW. PubMed=6277165 [NCBI, ExPASy, EBI, Israel, Japan] Benkovic S.J., Demaine M.M.; "Mechanism of action of fructose 1,6-bisphosphatase."; Adv. Enzymol. Relat. Areas Mol. Biol. 53:45-82(1982).
[5]	X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS), AND SEQUENCE REVISION. DOI=10.1016/0022-2836(90)90329-K; PubMed=2157849 [NCBI, ExPASy, EBI, Israel, Japan] Ke H.M., Thorpe C.M., Seaton B.A., Lipscomb W.N., Marcus F.; "Structure refinement of fructose-1,6-bisphosphatase and its fructose 2,6-bisphosphate complex at 2.8-A resolution."; J. Mol. Biol. 212:513-539(1990).
[6]	X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS). PubMed=2164670 [NCBI, ExPASy, EBI, Israel, Japan] Ke H.M., Zhang Y.P., Lipscomb W.N.; "Crystal structure of fructose-1,6-bisphosphatase complexed with fructose 6-phosphate, AMP, and magnesium."; Proc. Natl. Acad. Sci. U.S.A. 87:5243-5247(1990).
[7]	X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS). PubMed=1849642 [NCBI, ExPASy, EBI, Israel, Japan] Ke H.M., Zhang Y.P., Liang J.-Y., Lipscomb W.N.; "Crystal structure of the neutral form of fructose-1,6-bisphosphatase complexed with the product fructose 6-phosphate at 2.1-A resolution."; Proc. Natl. Acad. Sci. U.S.A. 88:2989-2993(1991).
[8]	X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS). PubMed=1312721 [NCBI, ExPASy, EBI, Israel, Japan] Liang J.-Y., Huang S., Zhang Y.P., Ke H.M., Lipscomb W.N.; "Crystal structure of the neutral form of fructose 1,6-bisphosphatase complexed with regulatory inhibitor fructose 2,6-bisphosphate at 2.6-A resolution."; Proc. Natl. Acad. Sci. U.S.A. 89:2404-2408(1992).
[9]	X-RAY CRYSTALLOGRAPHY (2.27 ANGSTROMS). DOI=10.1021/bi981112u; PubMed=9708979 [NCBI, ExPASy, EBI, Israel, Japan] Choe J.Y., Poland B.W., Fromm H.J., Honzatko R.B.; "Role of a dynamic loop in cation activation and allosteric regulation of recombinant porcine fructose-1,6-bisphosphatase."; Biochemistry 37:11441-11450(1998).
[10]	X-RAY CRYSTALLOGRAPHY (2.23 ANGSTROMS). DOI=10.1021/bi000574g; PubMed=10913263 [NCBI, ExPASy, EBI, Israel, Japan] Choe J.Y., Fromm H.J., Honzatko R.B.; "Crystal structures of fructose 1,6-bisphosphatase: mechanism of catalysis and allosteric inhibition revealed in product complexes."; Biochemistry 39:8565-8574(2000).

Comments

CATALYTIC ACTIVITY: D-fructose 1,6-bisphosphate + H₂O = D-fructose 6-phosphate + phosphate.
ENZYME REGULATION: Inhibited by AMP, which affects the turnover of bound substrate and not the affinity for substrate.
PATHWAY: Carbohydrate biosynthesis; gluconeogenesis .
SUBUNIT: Homotetramer. With four binding sites each for the substrate, for AMP, and for divalent metal cation (the greatest affinity is for zinc).
MISCELLANEOUS: The molecule has a highly reactive cysteine residue (Cys-117 or Cys-129), which tends to form mixed disulfides (e.g., with homocystine) but is not essential for enzyme activity.
SIMILARITY: Belongs to the FBPase class 1 family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

M86347; AAA31035.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

S37696; PAPGF.

NP_999144.1; -.

3D structure databases

PDB

1CNQ; X-ray; 2.27 A; A=1-338.	[ExPASy / RCSB / EBI]
1EYI; X-ray; 2.32 A; A=1-338.	[ExPASy / RCSB / EBI]
1EYJ; X-ray; 2.28 A; A/B=1-338.	[ExPASy / RCSB / EBI]
1EYK; X-ray; 2.23 A; A/B=1-338.	[ExPASy / RCSB / EBI]
1FBC; X-ray; 2.60 A; A/B=1-336.	[ExPASy / RCSB / EBI]
1FBD; X-ray; 2.90 A; A/B=1-336.	[ExPASy / RCSB / EBI]
1FBE; X-ray; 3.00 A; A/B=1-336.	[ExPASy / RCSB / EBI]
1FBF; X-ray; 2.70 A; A/B=1-336.	[ExPASy / RCSB / EBI]
1FBG; X-ray; 3.00 A; A/B=1-336.	[ExPASy / RCSB / EBI]
1FBH; X-ray; 2.50 A; A/B=1-336.	[ExPASy / RCSB / EBI]
1FBP; X-ray; 2.50 A; A/B=1-336.	[ExPASy / RCSB / EBI]
1FJ6; X-ray; 2.50 A; A=1-338.	[ExPASy / RCSB / EBI]
1FJ9; X-ray; 2.50 A; A/B=1-338.	[ExPASy / RCSB / EBI]
1FPB; X-ray; 2.60 A; A/B=1-336.	[ExPASy / RCSB / EBI]
1FPD; X-ray; 2.10 A; A/B=1-336.	[ExPASy / RCSB / EBI]
1FPE; X-ray; 2.20 A; A/B=1-336.	[ExPASy / RCSB / EBI]
1FPF; X-ray; 2.10 A; A/B=1-336.	[ExPASy / RCSB / EBI]
1FPG; X-ray; 2.30 A; A/B=1-336.	[ExPASy / RCSB / EBI]
1FPI; X-ray; 2.30 A; A/B=1-336.	[ExPASy / RCSB / EBI]
1FPJ; X-ray; 2.20 A; A/B=1-336.	[ExPASy / RCSB / EBI]
1FPK; X-ray; 3.00 A; A/B=1-336.	[ExPASy / RCSB / EBI]
1FPL; X-ray; 2.30 A; A/B=1-336.	[ExPASy / RCSB / EBI]
1FRP; X-ray; 2.00 A; A/B=1-336.	[ExPASy / RCSB / EBI]
1FSA; X-ray; 2.30 A; A/B=1-338.	[ExPASy / RCSB / EBI]
1KZ8; X-ray; 2.00 A; A/F=1-338.	[ExPASy / RCSB / EBI]
1LEV; X-ray; 2.15 A; A/F=1-338.	[ExPASy / RCSB / EBI]
1NUW; X-ray; 1.30 A; A=1-338.	[ExPASy / RCSB / EBI]
1NUX; X-ray; 1.60 A; A=1-338.	[ExPASy / RCSB / EBI]
1NUY; X-ray; 1.30 A; A=1-338.	[ExPASy / RCSB / EBI]
1NUZ; X-ray; 1.90 A; A=1-338.	[ExPASy / RCSB / EBI]
1NV0; X-ray; 1.80 A; A=1-338.	[ExPASy / RCSB / EBI]
1NV1; X-ray; 1.90 A; A=1-338.	[ExPASy / RCSB / EBI]
1NV2; X-ray; 2.10 A; A=1-338.	[ExPASy / RCSB / EBI]
1NV3; X-ray; 2.00 A; A=1-338.	[ExPASy / RCSB / EBI]
1NV4; X-ray; 1.90 A; A=1-338.	[ExPASy / RCSB / EBI]
1NV5; X-ray; 1.90 A; A=1-338.	[ExPASy / RCSB / EBI]
1NV6; X-ray; 2.15 A; A=1-338.	[ExPASy / RCSB / EBI]
1NV7; X-ray; 2.15 A; A/B=1-338.	[ExPASy / RCSB / EBI]
1Q9D; X-ray; 2.35 A; A/B=1-338.	[ExPASy / RCSB / EBI]
1RDX; X-ray; 2.75 A; A/B=1-338.	[ExPASy / RCSB / EBI]
1RDY; X-ray; 2.20 A; A/B=1-338.	[ExPASy / RCSB / EBI]
1RDZ; X-ray; 2.05 A; A/B=1-338.	[ExPASy / RCSB / EBI]
1YXI; X-ray; 2.00 A; A=1-338.	[ExPASy / RCSB / EBI]
1YYZ; X-ray; 1.85 A; A=1-338.	[ExPASy / RCSB / EBI]
1YZ0; X-ray; 2.07 A; A/B=1-338.	[ExPASy / RCSB / EBI]
2F3B; X-ray; 1.80 A; A=1-338.	[ExPASy / RCSB / EBI]
2F3D; X-ray; 1.83 A; A=1-338.	[ExPASy / RCSB / EBI]
2F3H; X-ray; 2.70 A; A/B=1-338.	[ExPASy / RCSB / EBI]
2FBP; X-ray; 2.80 A; A/B=1-336.	[ExPASy / RCSB / EBI]
2QVU; X-ray; 1.50 A; A/B=2-338.	[ExPASy / RCSB / EBI]
2QVV; X-ray; 2.03 A; A/B=2-338.	[ExPASy / RCSB / EBI]
3FBP; X-ray; 2.80 A; A/B=1-336.	[ExPASy / RCSB / EBI]
4FBP; X-ray; 2.50 A; A/B/C/D=1-336.	[ExPASy / RCSB / EBI]
5FBP; X-ray; 2.10 A; A/B=1-336.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1CNQ; -.
1EYI; -.
1EYJ; -.
1EYK; -.
1FBC; -.
1FBD; -.
1FBE; -.
1FBF; -.
1FBG; -.
1FBH; -.
1FBP; -.
1FJ6; -.
1FJ9; -.
1FPB; -.
1FPD; -.
1FPE; -.
1FPF; -.
1FPG; -.
1FPI; -.
1FPJ; -.
1FPK; -.
1FPL; -.
1FRP; -.
1FSA; -.
1KZ8; -.
1LEV; -.
1NUW; -.
1NUX; -.
1NUY; -.
1NUZ; -.
1NV0; -.
1NV1; -.
1NV2; -.
1NV3; -.
1NV4; -.
1NV5; -.
1NV6; -.
1NV7; -.
1Q9D; -.
1RDX; -.
1RDY; -.
1RDZ; -.
1YXI; -.
1YYZ; -.
1YZ0; -.
2F3B; -.
2F3D; -.
2F3H; -.
2FBP; -.
2QVU; -.
2QVV; -.
3FBP; -.
4FBP; -.
5FBP; -.

ModBase

P00636.

Ontologies

GO:0042132;	Molecular function: fructose 1,6-bisphosphate 1-phosphatase activity (inferred from electronic annotation from EC).
GO:0008270;	Molecular function: zinc ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0006094;	Biological process: gluconeogenesis (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR000146; In_FB_phphtase.
Graphical view of domain structure.

PANTHER

PTHR11556; In_FB_phphtase; 1.

Pfam

PF00316; FBPase; 1.
Pfam graphical view of domain structure.

PRINTS

PR00115; FBPHPHTASE.
PR00377; INFBPHPHTASE.

ProDom

PD001491; In_FB_phphtase; 1.
[Domain structure / List of seq. sharing at least 1 domain]

PS00124; FBPASE; 1.

Genome annotation databases

GeneID

397038; -.

KEGG

ssc:397038; -.

Phylogenomic databases

HOVERGEN

P00636; -.

Other

DrugBank

DB00131; Adenosine monophosphate.

LinkHub

P00636; -.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Acetylation; Allosteric enzyme; Carbohydrate metabolism; Direct protein sequencing; Gluconeogenesis; Hydrolase; Phosphoprotein; Zinc.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed.`
`CHAIN`	`2 338`	`337`	`Fructose-1,6-bisphosphatase 1.`	`PRO_0000200500`
`ACT_SITE`	`275 275`
`BINDING`	`142 142`		`Allosteric inhibitor.`
`MOD_RES`	`2 2`		`N-acetylthreonine.`
`MOD_RES`	`208 208`		`Phosphoserine; by PKA.`
`CONFLICT`	`2 2`		`T -> A (in Ref. 3; AA sequence).`
`CONFLICT`	`4 4`		`Q -> E (in Ref. 3; AA sequence).`
`CONFLICT`	`21 21`		`E -> Q (in Ref. 2; AA sequence).`
`CONFLICT`	`97 97`		`S -> T (in Ref. 2; AA sequence).`
`CONFLICT`	`157 157`		`G -> E (in Ref. 2; AA sequence).`
`CONFLICT`	`200 200`		`D -> N (in Ref. 2; AA sequence).`
`CONFLICT`	`229 229`		`Q -> E (in Ref. 2; AA sequence).`
`HELIX`	`14 24`	`11`
`HELIX`	`30 50`	`21`
`TURN`	`51 56`	`6`
`STRAND`	`59 64`	`6`
`STRAND`	`70 72`	`3`
`HELIX`	`73 88`	`16`
`STRAND`	`92 97`	`6`
`HELIX`	`108 110`	`3`
`STRAND`	`111 122`	`12`
`HELIX`	`124 126`	`3`
`TURN`	`127 130`	`4`
`STRAND`	`133 141`	`9`
`HELIX`	`150 153`	`4`
`HELIX`	`157 159`	`3`
`STRAND`	`161 178`	`18`
`STRAND`	`181 188`	`8`
`TURN`	`189 192`	`4`
`STRAND`	`193 198`	`6`
`STRAND`	`208 211`	`4`
`HELIX`	`214 219`	`6`
`HELIX`	`222 232`	`11`
`HELIX`	`249 259`	`11`
`STRAND`	`262 265`	`4`
`STRAND`	`275 277`	`3`
`TURN`	`278 281`	`4`
`HELIX`	`282 291`	`10`
`STRAND`	`295 297`	`3`
`STRAND`	`299 302`	`4`
`HELIX`	`303 305`	`3`
`STRAND`	`317 320`	`4`
`HELIX`	`322 334`	`13`

Sequence information

Length: 338 AA [This is the length of the unprocessed precursor]

Molecular weight: 36779 Da [This is the MW of the unprocessed precursor]

CRC64: 610BF8D3C6D320F6 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTDQAAFDTN IVTLTRFVME EGRKARGTGE MTQLLNSLCT AVKAISTAVR KAGIAHLYGI 

        70         80         90        100        110        120 
AGSTNVTGDQ VKKLDVLSND LVINVLKSSF ATCVLVSEED KNAIIVEPEK RGKYVVCFDP 

       130        140        150        160        170        180 
LDGSSNIDCL VSIGTIFGIY RKNSTDEPSE KDALQPGRNL VAAGYALYGS ATMLVLAMVN 

       190        200        210        220        230        240 
GVNCFMLDPA IGEFILVDRD VKIKKKGSIY SINEGYAKEF DPAITEYIQR KKFPPDNSAP 

       250        260        270        280        290        300 
YGARYVGSMV ADVHRTLVYG GIFMYPANKK SPKGKLRLLY ECNPMAYVME KAGGLATTGK 

       310        320        330 
EAVLDIVPTD IHQRAPIILG SPEDVTELLE IYQKHAAK

P00636 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools